Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity

Proceedings of the National Academy of Sciences of the United States of America

Volumn 105, Issue 39, 2008, Pages 14808-14813

  Sarkar, Casim A ^a,c   Dodevski, Igor ^a   Kenig, Manca ^a,d   Dudli, Stefan ^a   Mohr, Anja ^a   Hermans, Emmanuel ^b   Plückthun, Andreas ^a  

^a UNIVERSITY OF ZURICH   (Switzerland)

^b UNIVERSITÉ CATHOLIQUE DE LOUVAIN   (Belgium)

^c UNIVERSITY OF PENNSYLVANIA   (United States)

^d Lek Pharmaceuticals   (Slovenia)

Author keywords

Integral membrane proteins; Protein engineering; Protein folding

Indexed keywords

G PROTEIN COUPLED RECEPTOR; NEUROTENSIN RECEPTOR; NEUROTENSIN TYPE 1 RECEPTOR;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; EMBRYO; ESCHERICHIA COLI; HUMAN; HUMAN CELL; NONHUMAN; PHYSICAL CHEMISTRY; PICHIA PASTORIS; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN ENGINEERING; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN STABILITY; WILD TYPE; ANIMAL; BIOSYNTHESIS; CELL LINE; DIRECTED MOLECULAR EVOLUTION; GENETIC SELECTION; GENETICS; INTRACELLULAR MEMBRANE; METABOLISM; METHODOLOGY; MOLECULAR CLONING; MUTATION; PICHIA; RAT;

ESCHERICHIA COLI; EUKARYOTA; MAMMALIA; PICHIA PASTORIS;

ANIMALS; CELL LINE; CLONING, MOLECULAR; DIRECTED MOLECULAR EVOLUTION; ESCHERICHIA COLI; HUMANS; INTRACELLULAR MEMBRANES; MUTATION; PICHIA; PROTEIN ENGINEERING; RATS; RECEPTORS, G-PROTEIN-COUPLED; RECEPTORS, NEUROTENSIN; SELECTION (GENETICS);

EID: 54449087770     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0803103105     Document Type: Article

References (34)

1. Lundström K (2005) Structural genomics of GPCRs. Trends Biotechnol 23:103-108.
2. Berman HM, et al. (2000) The Protein Data Bank. Nucleic Acids Res 28:235-242.
3. Palczewski K, et al. (2000) Crystal structure of rhodopsin: A G protein-coupled receptor. Science 289:739-745.
4. Okada T, et al. (2000) X-ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles. J Struct Biol 130:73-80.
5. 2 adrenergic G-protein-coupled receptor. Nature 450:383-387.
6. 2-adrenergic G protein-coupled receptor. Science 318:1258-1265.
7. Sarramegna V, Talmont F, Demange P, Milon A (2003) Heterologous expression of G-protein-coupled receptors: Comparison of expression systems from the standpoint of large-scale production and purification. Cell Mol Life Sci 60:1529-1546.
8. Chen G, et al. (2001) Isolation of high-affinity ligand-binding proteins by periplasmic expression with cytometric screening (PECS). Nat Biotechnol 19:537-542.
9. Harvey BR, et al. (2004) Anchored periplasmic expression, a versatile technology for the isolation of high-affinity antibodies from Escherichia coli-expressed libraries. Proc Natl Acad Sci USA 101:9193-9198.
10. Grisshammer R, Duckworth R, Henderson R (1993) Expression of a rat neurotensin receptor in Escherichia coli. Biochem J 295:571-576.
11. Tucker J, Grisshammer R (1996) Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem J 317:891-899.
12. Zhao H, Giver L, Shao Z, Affholter JA, Arnold FH (1998) Molecular evolution by staggered extension process (StEP) in vitro recombination. Nat Biotechnol 16:258-261.
13. Gully D, et al. (1993) Biochemical and pharmacological profile of a potent and selective nonpeptide antagonist of the neurotensin receptor. Proc Natl Acad Sci USA 90:65-69.
14. i1 protein subunits promotes high-affinity agonist binding to the neurotensin receptor NTS-1 expressed in Escherichia coli. FEBS Lett 493:101-105.
15. Rovati GE, Capra V, Neubig RR (2007) The highly conserved DRY motif of class A G protein-coupled receptors: Beyond the ground state. Mol Pharmacol 71:959-964.
16. Julius D, Schekman R, Thorner J (1984) Glycosylation and processing of prepro-α-factor through the yeast secretory pathway. Cell 36:309-318.
17. Shusta EV, Kieke MC, Parke E, Kranz DM, Wittrup KD (1999) Yeast polypeptide fusion surface display levels predict thermal stability and soluble secretion efficiency. J Mol Biol 292:949-956.
18. Kimchi-Sarfaty C, et al. (2007) A "silent" polymorphism in the MDR1 gene changes substrate specificity. Science 315:525-528.
19. Lin-Chao S, Chen WT, Wong TT (1992) High copy number of the pUC plasmid results from a Rom/Rop-suppressible point mutation in RNA II. Mol Microbiol 6:3385-3393.
20. Labbe-Jullie C, et al. (1998) Mutagenesis and modeling of the neurotensin receptor NTR1: Identification of residues that are critical for binding SR 48692, a nonpeptide neurotensin antagonist. J Biol Chem 273:16351-16357.
21. 358 in helix seven. Br J Pharmacol 135:997-1002.
22. Ault AD, Broach JR (2006) Creation of GPCR-based chemical sensors by directed evolution in yeast. Protein Eng Des Sel 19:1-8.
23. Sommers CM, et al. (2000) A limited spectrum of mutations causes constitutive activation of the yeast α-factor receptor. Biochemistry 39:6898-6909.
24. Newstead S, Kim H, von Heijne G, Iwata S, Drew D (2007) High-throughput fluorescent-based optimization of eukaryotic membrane protein overexpression and purification in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 104:13936-13941.
25. Li B, et al. (2007) Rapid identification of functionally critical amino acids in a G protein-coupled receptor. Nat Methods 4:169-174.
26. Scarselli M, Li B, Kim SK, Wess J (2007) Multiple residues in the second extracellular loop are critical for M3 muscarinic acetylcholine receptor activation. J Biol Chem 282:7385-7396.
27. Sommers CM, Dumont ME (1997) Genetic interactions among the transmembrane segments of the G protein coupled receptor encoded by the yeast STE2 gene. J Mol Biol 266:559-575.
28. Molina DM, et al. (2008) Engineering membrane protein overproduction in Escherichia coli. Protein Sci 17:673-680.
29. Serrano-Vega MJ, Magnani F, Shibata Y, Tate CG (2008) Conformational thermostabilization of the β1-adrenergic receptor in a detergent-resistant form. Proc Natl Acad Sci USA 105:877-882.
30. Grisshammer R, Tucker J (1997) Quantitative evaluation of neurotensin receptor purification by immobilized metal affinity chromatography. Protein Expr Purif 11:53-60.
31. DuBridge RB, et al. (1987) Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Mol Cell Biol 7:379-387.
32. Ott D, Frischknecht R, Plückthun A (2004) Construction and characterization of a kappa opioid receptor devoid of all free cysteines. Protein Eng Des Sel 17:37-48.
33. Vermeiren C, et al. (2006) Loss of metabotropic glutamate receptor-mediated regulation of glutamate transport in chemically activated astrocytes in a rat model of amyotrophic lateral sclerosis. J Neurochem 96:719-731.
34. Talmont F, Sidobre S, Demange P, Milon A, Emorine LJ (1996) Expression and pharmacological characterization of the human μ-opioid receptor in the methylotrophic yeast Pichia pastoris. FEBS Lett 394:268-272.